1fqj: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
No edit summary
OCA (talk | contribs)
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
{{Seed}}
[[Image:1fqj.png|left|200px]]


<!--
==CRYSTAL STRUCTURE OF THE HETEROTRIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, THE GAMMA SUBUNIT OF PHOSPHODIESTERASE AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(PDEGAMMA)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]==
The line below this paragraph, containing "STRUCTURE_1fqj", creates the "Structure Box" on the page.
<StructureSection load='1fqj' size='340' side='right'caption='[[1fqj]], [[Resolution|resolution]] 2.02&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1fqj]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FQJ FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.02&#8491;</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALF:TETRAFLUOROALUMINATE+ION'>ALF</scene>, <scene name='pdbligand=GDP:GUANOSINE-5-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></td></tr>
{{STRUCTURE_1fqj|  PDB=1fqj  |  SCENE=  }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fqj OCA], [https://pdbe.org/1fqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fqj RCSB], [https://www.ebi.ac.uk/pdbsum/1fqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fqj ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/GNAT1_BOVIN GNAT1_BOVIN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. Transducin is an amplifier and one of the transducers of a visual impulse that performs the coupling between rhodopsin and cGMP-phosphodiesterase.[https://www.uniprot.org/uniprot/GNAI1_RAT GNAI1_RAT] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(i) proteins are involved in hormonal regulation of adenylate cyclase: they inhibit the cyclase in response to beta-adrenergic stimuli. The inactive GDP-bound form prevents the association of RGS14 with centrosomes and is required for the translocation of RGS14 from the cytoplasm to the plasma membrane. May play a role in cell division.<ref>PMID:16870394</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/fq/1fqj_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1fqj ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
A multitude of heptahelical receptors use heterotrimeric G proteins to transduce signals to specific effector target molecules. The G protein transducin, Gt, couples photon-activated rhodopsin with the effector cyclic GMP phosophodiesterase (PDE) in the vertebrate phototransduction cascade. The interactions of the Gt alpha-subunit (alpha(t)) with the inhibitory PDE gamma-subunit (PDEgamma) are central to effector activation, and also enhance visual recovery in cooperation with the GTPase-activating protein regulator of G-protein signalling (RGS)-9 (refs 1-3). Here we describe the crystal structure at 2.0 A of rod transducin alpha x GDP x AlF4- in complex with the effector molecule PDEgamma and the GTPase-activating protein RGS9. In addition, we present the independently solved crystal structures of the RGS9 RGS domain both alone and in complex with alpha(t/i1) x GDP x AlF4-. These structures reveal insights into effector activation, synergistic GTPase acceleration, RGS9 specificity and RGS activity. Effector binding to a nucleotide-dependent site on alpha(t) sequesters PDEgamma residues implicated in PDE inhibition, and potentiates recruitment of RGS9 for hydrolytic transition state stabilization and concomitant signal termination.


===CRYSTAL STRUCTURE OF THE HETEROTRIMERIC COMPLEX OF THE RGS DOMAIN OF RGS9, THE GAMMA SUBUNIT OF PHOSPHODIESTERASE AND THE GT/I1 CHIMERA ALPHA SUBUNIT [(RGS9)-(PDEGAMMA)-(GT/I1ALPHA)-(GDP)-(ALF4-)-(MG2+)]===
Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 A.,Slep KC, Kercher MA, He W, Cowan CW, Wensel TG, Sigler PB Nature. 2001 Feb 22;409(6823):1071-7. PMID:11234020<ref>PMID:11234020</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1fqj" style="background-color:#fffaf0;"></div>


<!--
==See Also==
The line below this paragraph, {{ABSTRACT_PUBMED_11234020}}, adds the Publication Abstract to the page
*[[Regulator of G-protein signaling 3D structures|Regulator of G-protein signaling 3D structures]]
(as it appears on PubMed at http://www.pubmed.gov), where 11234020 is the PubMed ID number.
*[[Transducin 3D structures|Transducin 3D structures]]
-->
== References ==
{{ABSTRACT_PUBMED_11234020}}
<references/>
 
__TOC__
==About this Structure==
</StructureSection>
1FQJ is a 5 chains structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus_and_rattus_norvegicus Bos taurus and rattus norvegicus] and [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FQJ OCA].
 
==Reference==
<ref group="xtra">PMID:11234020</ref><references group="xtra"/>
[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Bos taurus and rattus norvegicus]]
[[Category: Large Structures]]
[[Category: Cowan, C W.]]
[[Category: Rattus norvegicus]]
[[Category: He, W.]]
[[Category: Cowan CW]]
[[Category: Kercher, M A.]]
[[Category: He W]]
[[Category: Sigler, P B.]]
[[Category: Kercher MA]]
[[Category: Slep, K C.]]
[[Category: Sigler PB]]
[[Category: Wensel, T G.]]
[[Category: Slep KC]]
[[Category: Effector]]
[[Category: Wensel TG]]
[[Category: G protein]]
[[Category: Gap]]
[[Category: Pdegamma]]
[[Category: Phosphodiesterase]]
[[Category: Phototransduction]]
[[Category: Rg]]
[[Category: Rgs9]]
[[Category: Rod]]
[[Category: Transducin]]
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 05:09:59 2009''